Hi Frank,
Once we could not crystallize a monomer protein, but we knew the
structure of a homolog dimer. We made some educated guessed mutations to
dimerize our monomer target, which were based on the structure of the
dimeric homolog. Perhaps evidence or perhaps just luck? :-)
https://pubmed.ncbi.nlm.nih.gov/22868772/
BW,
D
On 12/11/2021 14:58, Srivastava, Dhiraj wrote:
Recently there were few articles where synthetic symmetrization was
used to enhance the crystallizability. proteins used were MBP,
lysozyme and GFP to name a few. you can search for it. one of them is -
https://www.sciencedirect.com/science/article/pii/S0969212615002890
<https://www.sciencedirect.com/science/article/pii/S0969212615002890>
A Suite of Engineered GFP Molecules for Oligomeric Scaffolding
<https://www.sciencedirect.com/science/article/pii/S0969212615002890>
Applications ranging from synthetic biology to protein crystallization
could be advanced by facile systems for connecting multiple proteins
together i…
www.sciencedirect.com
Dhiraj
------------------------------------------------------------------------
*From:* CCP4 bulletin board <CCP4BB@JISCMAIL.AC.UK> on behalf of Frank
von Delft <frank.vonde...@cmd.ox.ac.uk>
*Sent:* Friday, November 12, 2021 8:52 AM
*To:* CCP4BB@JISCMAIL.AC.UK <CCP4BB@JISCMAIL.AC.UK>
*Subject:* [External] [ccp4bb] High-order oligomers vs robust crystals
- references?
Hello all
Two decades ago, I remember (!) much talk about a reason that bacterial
proteins crystallize "more easily" is that they tend to come as
oligomers (dimers and up), and that this internal symmetry made them
happier to crystallize.
Did anybody ever publish hard evidence? Or even, is there a primary
citation for the idea?
Thanks
Frank
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--
Dom Bellini, Xray Crystallography Facility (1S205)
MRC Laboratory of Molecular Biology
Francis Crick Avenue
Cambridge Biomedical Campus
Cambridge CB2 0QH
Phone 01223 267839
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